Physical Biochemistry: Principles and Applications / Edition 2

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Overview

"As will be seen, there is not much missing here. I thought that the sections were well balanced, with rarely too much or too little on a given topic...This is a text to be welcomed by both teachers and students." BIOCHEMISTRY & MOLECULAR BIOLOGY EDUCATION (on the first edition)

The second edition of this successful textbook explains the basic principles behind the key techniques currently used in the modern biochemical laboratory and describes the pros and cons of each technique and compares one to another. It is non-mathematical, comprehensive and approachable for students who are not physical chemists.

  • A major update of this comprehensive, accessible introduction to physical biochemistry.
  • Includes two new chapters on proteomics and bioinformatics.
  • Introduces experimental approaches with a minimum of mathematics and numerous practical examples.
  • Provides a bibliography at the end of each chapter.

Written by an author with many years teaching and research experience, this text is a must-have for students of biochemistry, biophysics, molecular and life sciences and food science.

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Editorial Reviews

Booknews
This undergraduate text offers an overview of the techniques used to characterize the structure and function of complex biomacromolecules such as proteins and DNA. Sheehan (biochemistry, University College Cork) covers topics such as chromatography, spectroscopy, electrophoresis, X-ray diffraction, and biocalorimetry, explaining the physical principles upon which these developments depend, and comparing the differences and similarities of these experimental procedures. Annotation c. Book News, Inc., Portland, OR (booknews.com)
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Product Details

  • ISBN-13: 9780470856031
  • Publisher: Wiley
  • Publication date: 5/26/2009
  • Edition description: Revised Edition
  • Edition number: 2
  • Pages: 424
  • Product dimensions: 7.40 (w) x 9.60 (h) x 1.00 (d)

Table of Contents

Preface
Acknowledgements
Ch. 1 Introduction 1
1.1 Special chemical requirements of biomolecules 1
1.2 Factors affecting analyte structure and stability 3
1.3 Buffering systems used in biochemistry 7
1.4 Quantitation, units and data handling 9
1.5 Objectives of this book 10
Ch. 2 Chromatography 12
2.1 Principles of chromatography 12
2.2 Performance parameters used in chromatography 16
2.3 Chromatography equipment 23
2.4 Modes of chromatography 26
2.5 Open-column chromatography 44
2.6 High-performance liquid chromatography 46
2.7 Fast protein liquid chromatography 50
2.8 Perfusion chromatography 51
2.9 Membrane-based chromatography systems 54
2.10 Chromatography of a sample protein 55
Ch. 3 Spectroscopic Techniques 61
3.1 The nature of light 61
3.2 The electromagnetic spectrum 65
3.3 Ultraviolet/visible absorption spectroscopy 66
3.4 Fluorescence spectroscopy 74
3.5 Spectroscopic techniques using plane-polarised light 88
3.6 Infrared spectroscopy 95
3.7 Nuclear magnetic resonance (NMR) spectroscopy 103
3.8 Electron spin resonance (ESR) spectroscopy 109
3.9 Lasers 113
Ch. 4 Mass spectrometry 121
4.1 Principles of mass spectrometry 121
4.2 Mass spectrometry of proteins and peptides 134
4.3 Interfacing MS with other methods 135
4.4 Uses of mass spectrometry in biochemistry 138
Ch. 5 Electrophoresis 153
5.1 Principles of electrophoresis 153
5.2 Non-denaturing electrophoresis 160
5.3 Denaturing electrophoresis 164
5.4 Electrophoresis in DNA sequencing 169
5.5 Isoelectric focusing (IEF) 177
5.6 Two-dimensional SDS page 183
5.7 Immunoelectrophoresis 186
5.8 Agarose gel electro-phoresis of nucleic acids 190
5.9 Pulsed field gel electrophoresis 193
5.10 Capillary electrophoresis 197
5.11 Electroblotting procedures 204
5.12 Electroporation of cells 211
Ch. 6 Three-dimensional structure determination of macromolecules 215
6.1 The protein-folding problem 216
6.2 Structure determination by NMR 230
6.3 Crystallisation of biomacromolecules 245
6.4 X-ray diffraction by crystals 257
6.5 Calculation of electron density maps 263
6.6 Other diffraction methods 279
6.7 Comparison of X-ray crystallography with multi-dimensional NMR 281
6.8 Structural databases 282
Ch. 7 Hydrodynamic methods 287
7.1 Viscosity 287
7.2 Sedimentation 292
7.3 Methods for varying buffer conditions 305
7.4 Flow cytometry 310
Ch. 8 Biocalorimetry 317
8.1 The main thermodynamic parameters 318
8.2 Isothermal titration calorimetry 321
8.3 Differential scanning calorimetry 323
8.4 Determination of thermodynamic parameters by non-calorimetric means 326
App. 1 SI units 329
App. 2 The Fourier transform 330
Index 335
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